Tau protein: Relevance to Parkinson's disease

被引:148
作者
Lei, Peng [1 ,3 ]
Ayton, Scott [2 ,4 ]
Finkelstein, David I. [2 ,4 ]
Adlard, Paul A. [1 ,2 ,3 ]
Masters, Colin L. [1 ]
Bush, Ashley I. [1 ,3 ]
机构
[1] Mental Hlth Res Inst, Oxidat Biol Lab, Parkville, Vic 3052, Australia
[2] Mental Hlth Res Inst, Synapt & Cognit Neuropathol Unit, Parkville, Vic 3052, Australia
[3] Univ Melbourne, Dept Pathol, Parkville, Vic 3010, Australia
[4] Univ Melbourne, Ctr Neurosci, Parkville, Vic 3010, Australia
基金
英国医学研究理事会; 澳大利亚研究理事会;
关键词
Tau; MAPT; Parkinson's disease; Alzheimer's disease; Axonal transport; ALPHA-SYNUCLEIN; AXONAL-TRANSPORT; LEWY BODIES; MAPT REGION; PHOSPHORYLATION; FIBRILLIZATION; COLOCALIZATION; ASSOCIATION; ALZHEIMERS; EPITOPES;
D O I
10.1016/j.biocel.2010.07.016
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Tau is a microtubule-associated protein linked with neurodegenerative diseases. Humans express six different isoforms of tau; the longest containing four microtubule-binding repeat motifs in the C-terminal that are vital for what is considered the major biological function of tau, to stabilize microtubules and facilitate axonal transport. The capacity of tau to maintain its normal biological function is dependent upon its phosphorylation state. In Alzheimer's and Parkinson's diseases, there is a hyperphosphorylation of tau that leads to the intracellular accumulation of tau in the form of neurofibrillary tangles. While the role of tau in Parkinson's disease has been understated for some time, here we summarize key genetic, pathological and biochemical evidence supporting a role for tau in the pathogenesis of Parkinson's disease. Toxic interactions with alpha synuclein may lead to hyperphosphorylation of tau and eventually to the deposition of both proteins in the disease. (C) 2010 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1775 / 1778
页数:4
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